Structural and spectroscopic insights into fucoxanthin chlorophyll a/c-binding proteins of diatoms in diverse oligomeric states  

作　　者：Cuicui Zhou Yue Feng Zhenhua Li Lili Shen Xiaoyi Li Yumei Wang Guangye Han Tingyun Kuang Cheng Liu Jian-Ren Shen Wenda Wang 

机构地区：[1]Photosynthesis Research Center,Key Laboratory of Photobiology,Institute of Botany,Chinese Academy of Sciences,Beijing 100093,P.R.China [2]University of the Chinese Academy of Sciences,Beijing 100049,P.R.China [3]China National Botanical Garden,Beijing 100093,P.R.China [4]Academician Workstation of the Agricultural High-Tech Industrial Area of the Yellow River Delta,National Center of Technology Innovation for Comprehensive Utilization of Saline-Alkali Land,Dongying 257300,P.R.China [5]Beijing National Laboratory for Condensed Matter Physics,Institute of Physics,Chinese Academy of Science,Beijing 100190,P.R.China [6]Research Institute for Interdisciplinary Science,Graduate School of Natural Science and Technology,Okayama University,Okayama 700-8530,Japan [7]These authors contributed equally to this article

出　　处：《Plant Communications》2024年第11期128-143,共16页植物通讯（英文）

基　　金：National Key R&D Program of China(2021YFA1300403 and 2019YFA0906300);Youth Innovation Promotion Association of CAS(2020081);CAS Interdisciplinary Innovation Team(JCTD-2020-06);CAS Project for Young Scientists in Basic Research(YSBR-004);National Natural Science Foundation of China(32222007);Innovation Platform for Academicians of Hainan Province(2022YSCXTD0005);Science&Technology Specific Project in Agricultural High-tech Industrial Demonstration Area of the Yellow River Delta(2022SZX12).

摘　　要：Diatoms,a group of prevalent marine algae,contribute significantly to global primary productivity.Their substantial biomass is linked to enhanced absorption of blue-green light underwater,facilitated by fucoxanthin chlorophyll(Chl)a/c-binding proteins(FCPs),which exhibit oligomeric diversity across diatom species.Using mild clear native PAGE analysis of solubilized thylakoid membranes,we displayed monomeric,dimeric,trimeric,tetrameric,and pentameric FCPs in diatoms.Mass spectrometry analysis revealed that each oligomeric FCP has a specific protein composition,and together they constitute a large Lhcf family of FCP antennas.In addition,we resolved the structures of the Thalassiosira pseudonana FCP(Tp-FCP)homotrimer and the Chaetoceros gracilis FCP(Cg-FCP)pentamer by cryoelectron microscopy at 2.73-Åand 2.65-Åresolution,respectively.The distinct pigment compositions and organizations of various oligomeric FCPs affect their blue-green light-harvesting,excitation energy transfer pathways.Compared with dimeric and trimeric FCPs,the Cg-FCP tetramer and Cg-FCP pentamer exhibit stronger absorption by Chl c,redshifted and broader Chl a fluorescence emission,and more robust circular dichroism signals originating from Chl a-carotenoid dimers.These spectroscopic characteristics indicate that Chl a molecules in the Cg-FCP tetramer and Cg-FCP pentamer are more heterogeneous than in both dimers and the Tp-FCP trimer.The structural and spectroscopic insights provided by this study contribute to a better understanding of the mechanisms that empower diatoms to adapt to fluctuating light environments.

关 键 词：DIATOMS fucoxanthin-chlorophyll a/c-binding proteins oligomeric diversity cryoelectron microscopy light harvesting pigment interaction 

分 类 号：Q94[生物学—植物学]